ArticleJournal of bacteriology2003
The crystal structure of the phosphorylation domain in PhoP reveals a functional tandem association mediated by an asymmetric interface.
Article in Journal of bacteriology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 49 citations in OpenAlex.
- Acetylation of PhoP K88 Is Involved in RegulatingInfection and immunity · 2021Article
- Characterization of a temperature-responsive two component regulatory system from the Antarctic archaeon, Methanococcoides burtonii.Scientific reports · 2016Article
- The aspartate-less receiver (ALR) domains: distribution, structure and function.PLoS pathogens · 2015Article
- Structural basis of a physical blockage mechanism for the interaction of response regulator PmrA with connector protein PmrD from Klebsiella pneumoniae.The Journal of biological chemistry · 2013Article
- Article
- Identification of DNA binding motifs of the Mycobacterium tuberculosis PhoP/PhoR two-component signal transduction system.PloS one · 2012Article
- Structure of the response regulator PhoP from Mycobacterium tuberculosis reveals a dimer through the receiver domain.Biochemistry · 2011Article
- The BatR/BatS two-component regulatory system controls the adaptive response of Bartonella henselae during human endothelial cell infection.Journal of bacteriology · 2010Article
- High-resolution protein complexes from integrating genomic information with molecular simulation.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Mycobacterium tuberculosis PhoP recognizes two adjacent direct-repeat sequences to form head-to-head dimers.Journal of bacteriology · 2009Article
- Probing the roles of the two different dimers mediated by the receiver domain of the response regulator PhoB.Journal of molecular biology · 2009Article
- Biological insights from structures of two-component proteins.Annual review of microbiology · 2009Article
- Structure of the DNA-binding domain of the response regulator PhoP from Mycobacterium tuberculosis.Biochemistry · 2007Article
- Crystal structures of the receiver domain of the response regulator PhoP from Escherichia coli in the absence and presence of the phosphoryl analog beryllofluoride.Journal of bacteriology · 2007Article
- Domain orientation in the inactive response regulator Mycobacterium tuberculosis MtrA provides a barrier to activation.Biochemistry · 2007Article
- The X-ray crystal structures of two constitutively active mutants of the Escherichia coli PhoB receiver domain give insights into activation.Journal of molecular biology · 2007Article
- Constitutive activation of two-component response regulators: characterization of VirG activation in Agrobacterium tumefaciens.Journal of bacteriology · 2006Article
- Mechanism of activation for transcription factor PhoB suggested by different modes of dimerization in the inactive and active states.Structure (London, England : 1993) · 2005Article
- Bacillus subtilis phosphorylated PhoP: direct activation of the E(sigma)A- and repression of the E(sigma)E-responsive phoB-PS+V promoters during pho response.Journal of bacteriology · 2005Article
- Structural analysis and solution studies of the activated regulatory domain of the response regulator ArcA: a symmetric dimer mediated by the alpha4-beta5-alpha5 face.Journal of molecular biology · 2005Article
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Authors and funding
4 authors at 2 institutions in 2 countries.
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Abstract
PhoP from Bacillus subtilis belongs to the OmpR subfamily of response regulators. It regulates the transcription of several operons and participates in a signal transduction network that controls adaptation of the bacteria to phosphate deficiency. The receiver domains of two members of this subfamily, PhoB from Escherichia coli and DrrD from Thermotoga maritima, have been structurally characterized. These modules have similar overall folds but display remarkable differences in the conformation of the beta4-alpha4 and alpha4 regions. The crystal structure of the receiver domain of PhoP (PhoPN) described in this paper illustrates yet another geometry in this region. Another major issue of the structure determination is the dimeric state of the protein and the novel mode of association between receiver domains. The protein-protein interface is provided by two different surfaces from each protomer, and the tandem unit formed through this asymmetric interface leaves free interaction surfaces. This design is well suited for further association of PhoP dimers to form oligomeric structures. The interprotein interface buries 970 A(2) from solvent and mostly involves interactions between charged residues. As described in the accompanying paper, mutations of a single residue in one salt bridge shielded from solvent prevented dimerization of the unphosphorylated and phosphorylated response regulator and had drastic functional consequences. The three structurally documented members of the OmpR family (PhoB, DrrD, and PhoP) provide a framework to consider possible relationships between structural features and sequence signatures in critical regions of the receiver domains.
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